• Korean Journal of Exercise Nutrition
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• v.24 no.2
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• pp.6-10
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• 2020

[Purpose] Milk is a commonly ingested post-exercise recovery protein source. Casein protein, found in milk, is characterized by its slow digestion and absorption. Recently, several studies have been conducted with a focus on how pre-sleep casein protein intake could affect post-exercise recovery but our knowledge of the subject remains limited. This review aimed at presenting and discussing how pre-sleep casein protein ingestion affects post-exercise recovery and the details of its potential effector mechanisms. [Methods] We systematically reviewed the topics of 1) casein nutritional characteristics, 2) pre-sleep casein protein effects on post-exercise recovery, and 3) potential effector mechanisms of pre-sleep casein protein on post-exercise recovery, based on the currently available published studies on pre-sleep casein protein ingestion. [Results] Studies have shown that pre-sleep casein protein ingestion (timing: 30 minutes before sleep, amount of casein protein ingested: 40-48 g) could help post-exercise recovery and positively affect acute protein metabolism and exercise performance. In addition, studies have suggested that repeated pre-sleep casein protein ingestion for post-exercise recovery over a long period might also result in chronic effects that optimize intramuscular physiological adaptation (muscle strength and muscle hypertrophy). The potential mechanisms of pre-sleep casein protein ingestion that contribute to these effects include the following: 1) significantly increasing plasma amino acid availability during sleep, thereby increasing protein synthesis, inhibiting protein breakdown, and achieving a positive protein balance; and 2) weakening exercise-induced muscle damage or inflammatory responses, causing reduced muscle soreness. Future studies should focus on completely elucidating these potential mechanisms. [Conclusion] In conclusion, post-exercise ingestion of at least 40 g of casein protein, approximately 30 minutes before sleep and after a bout of resistance exercise in the evening, might be an effective nutritional intervention to facilitate muscle recovery.

• Macromolecular Research
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• v.9 no.4
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• pp.197-205
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• 2001

Platelet adhesion onto elastic polymeric biomaterials was tested in vitro by perfusing human whole blood at a shear rate of 100 sec$\^$-1/ for possible verification of mechanisms of initial platelet adhesion perfusion of blood on the polymeric substrates was performed after treatments either with or without pre-adsorption of 1% blood plasma, and either with or without residence of the protein-preadsorbed substrate in phosphate buffered solution. The surfaces employed were elastic polymers such as poly(ether urethane urea), poly(ether urethane), silicone urethane copolymer, silicone rubber and poly(ether urethane) with the anti-calcifying agent hydroxyethane bisphosphate. Each polymer surface treated was exposed in vitro to the dynamic, heparinized whole blood perfused for upto 6 min and the surface area of platelets initially adhered was measured by employing in situ epifluorescence video microscopy. The blood perfusion was performed on the surfaces treated at the following three different conditions: directly on the bare surfaces, after protein pre-adsorption and after residence in buffer for 3 days of the surfaces protein pre-adsorbed for 2 h. The effects of blood plasma pre-adsorption on the initial platelet adhesion was surface-dependent. The amount of the adsorbed fibrinogen and the surface coverage area of the adhered platelets were dependent on the surface conditions whether substrates were bare surfaces or protein pre-adsorbed ones. To test an effect of possible morphological (re)orientations of the adsorbed proteins on the initial platelet adhesion, the polymeric substrate pre-adsorbed with 1% blood plasma was immersed in phosphate buffered solution for 3 days and then exposed to physiological blood perfusion. The surface area of the platelets adhered on these surfaces was significantly different from that of the surfaces treated with protein pre-adsorption only. These results indicated that platelet adhesion was dependent on the surface property itself and pre-treatment conditions such as blood perfusion without any pre-adsorption of proteins, and blood perfusion either after protein pre-adsorption or after subsequent substrate residence in buffer of the substrate pre-adsorbed with proteins. Understanding of these results may guide for better designs of blood-contacting materials based on protein behaviors.

• Microbiology and Biotechnology Letters
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• v.26 no.6
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• pp.566-568
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• 1998

Partial nucleotide sequence (nt 1-1842) of chloramphenicol resistance plasmid pKH7 has been reported previously and residual nucleotide sequence (nt 1843-4118) of pKH7 was determined and then the complete nucleotide sequence of pKH7 was obtained. pKH7 consists of 4118 bp and has three ORFs. Besides Rep and CAT proteins described in previous paper, Pre protein which mediates site-specific recombination in Staphylococcus aureus was found to be on pKH7. R $S_{A}$, a site-specific recombination site of Pre protein, and palA, a specific lagging-strand conversion signal, was also found in pKH7. Amino acid sequence of Pre protein of pKH7 was compared with those of other antibiotic resistant Staphylococcus aureus plasmids.s.

• Textile Coloration and Finishing
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• v.28 no.3
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• pp.208-218
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• 2016

This study investigated the effects of the working mechanisms of proteins, mordants, and dyes, as well as the mordanting order, on dye uptake by silk fabric pre-treated with proteins and dyed with freeze-dried sappan wood water extract. Soybean protein and sodium caseinate were used as the proteins. 1. When Al mordants were not used, the dyeability of the fabrics increased upon protein pre-treatment as compared to the case without treatment. 2. Dyeing with protein pre-treatment, followed by mordanting, led to the highest dye uptake, and the optimal protein concentration was 5%. 3. The K/S values slightly decreased with an increase in the dyeing temperature, and the fabric turned dark red in color when dyeing was carried out at increasing temperature. Fabrics showed the highest dye uptake at $40^{\circ}C$. 4. Regarding the effect of time, the K/S values of the fabrics with and without protein treatment showed almost no increase after the initial dyeing time of 10min; further, there was hardly any difference in the cases with and without protein pre-treatment. 5. In case of protein pre-treatment fabrics, the washing fastness was level 2. The dry cleaning fastness showed very excellent result with level 4-5. The rubbing fastness was better in dry rubbing than in wet rubbing of the fabrics. For the light fastness, all dyed fabrics showed low fastness.

• BMB Reports
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• v.29 no.2
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• pp.175-179
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• 1996

Viral surface proteins are known to play an essential role in attachment of the virus particle to the host cell membrane. In case of the hepatitis B virus (HBV) several reports have described potential receptors on the target cell side, but no definite receptor protein has been isolated yet. As for the viral side, it has been suggested that the preS region of the envelope protein, especially the preS1 region, is involved in binding of HBV to the host cell. In this study, preS1 region was recombinantly expressed in the form of a maltose binding protein (MBP) fusion protein and used to identify and visualize the expression of putative HBV receptor(s) on the host cell. Using laser scanned confocal microscopy and by FACS analysis, MBP-preS1 proteins were shown to bind to the human hepatoma cell line HepG2 in a receptor-ligand specific manner. The binding kinetic of MBP-preS1 to its cellular receptor was shown to be temperature and time dependent. In cells permeabilized with Triton X-100 and treated with the fusion protein, a specific staining of the nuclear membrane could be observed. To determine the precise location of the receptor binding site within the preS1 region, several short overlapping peptides from this region were synthesized and used in a competition assay. In this way the receptor binding epitope in preS1 was revealed to be amino acid residues 27 to 51, which is in agreement with previous reports. These results confirm the significance of the preS1 region in virus attachment in general, and suggest an internalization pathway mediated by direct attachment of the viral particle to the target cell membrane.

• BMB Reports
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• v.39 no.6
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• pp.717-721
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• 2006

In vitro analyses of type I signal peptidase activities require protein precursors as substrates. Usually, these pre-proteins are expressed in vitro and cleavage of the signal sequence is followed by SDS polyacrylamide gel electrophoresis coupled with autoradiography. Radioactive amino acids have to be incorporated in the expressed protein, since the amount of the in vitro expressed protein is usually very low and processing of the signal peptide cannot be followed by SDS polyacrylamide gel electrophoresis alone. Here we describe a rapid and simple method to express large amounts of a protein precursor in E. coli. We have analyzed the effect of ionophors as well as of azide on the accumulation of expressed protein precursors. Azide blocks the function of SecA and the ionophors dissipate the electrochemical gradient across the cytoplasmic membrane of E. coli. Addition of azide ions resulted in the formation of inclusion bodies, highly enriched with pre-apo-plastocyanine. Plastocyanine is a soluble copper protein, which can be found in the periplasmic space of cyanobacteria as well as in the thylakoid lumen of cyanobacteria and chloroplasts, and the pre-protein contains a cleavable signal sequence at its N-terminus. After purification of cyanobacterial pre-apo-plastocyanine, its signal sequence can be cleaved off by the E. coli signal peptidase, and protein processing was followed on Coomassie stained SDS polyacrylamide gels. We are optimistic that the presented method can be further developed and applied.

• Preventive Nutrition and Food Science
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• v.2 no.3
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• pp.225-231
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• 1997

Thirteen healthy control, 13 pre-eclamptic, 7 diabetic(DM) and 12 gestational diabetic(GDM) pregnant women participated in a study ofthe interrelationships between the levels of protein, calcium, magnesium, phosphorus, zinc and copper in urine. Urinary protein, magnesium and copper levels were significantly higher (p<0.0005, p<0.0003, p<0.005 respectively) in pre-eclamptic women than those of control, DM and GDM women. Urinary zinc excretion in pre-eclamptic women (1.61 mg/g creatinine) was higher than that of DM women (0.81mg/g creatinine); urinary zinc losses of control and GDM women were wre between the other two rups. The GDM women excreted significantly ore phosphorus in their urine in comparison to control and preeclamptic women (p<0.02), but this was not seen in DM women. Among the DM women, urinary protein excretion was positively correlated with glycosylated hemoglobin(r=0.940) and fasting blood glucose concentration (r=0.889). Urinary zinc excretion also was correlated with glycosylated hemoglobin (r=0.853) and fasting blood glucose (r=0.956). In the GDM and pre-eclamptic women there were also significant correlations between urinar calcium and magnesium (r=0.857, r=0.749 respectively) and between urinary protein and copper(r=0.638, r=0.778 respectively).

• Journal of Microbiology and Biotechnology
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• v.10 no.6
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• pp.844-850
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• 2000

The specific binding and internalization of viral particles is an essential step for the successful infection of viral pathogens. In the case of the hepatitis B virus (HBV), virions bind to the host cell via the preS domain of the viral surface antigen and are subsequently internalized by endocytosis. HBV-preS specific receptors are primarily expressed on hepatocytes, however, viral DNA and proteins have also been detected in extrahepatic sites, suggsting that celluar recepators for HBV may also exist on extrahepatic cells. Recently, an EBV-transformed B-cell line was identified onto which the preS region binds in a receptor-ligand specific manner. In this study, this specific interaction was further characterized, and the binding region within the preS protein was locaized. Also the internalization after host cell attachment was visualized and analyzed by fluorescence-labeled HBV-preS1 proteins using confocal microscopy. Energy depletion by sodium azide treatment effectively inhibited the internalization of the membrane-bound preS1 ligands, thereby indicating an energy-dependent receptor-mediated endocytotic pathway. Accordingly, the interaction of HBV-pres! with this specific B-cell line may serve as an effective model for an infection pathway in extrahepatic cells.

• YAKHAK HOEJI
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• v.45 no.6
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• pp.708-714
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• 2001

Many studies have provided evidences that hepatitis B surface antigen (HBsAg) including preS region could be an ideal candidate for a new hepatitis B virus (HBV) vaccine with higher efficacy. We established CHO cell lines, IY-CHO-2 and IY-CHO-11 expressing high levels of HBsAg containing preS2 and S protein by stable transfection method. These cell lines expressed the correct size (about 1 kb in length) of HBsAg mRNA as expected. The purified protein from the culture supernatants of the clones showed the same sizes as those expressed in native hepatitis B virus (24 kDa, 27 kDa, 34 kDa and 36 kDa). Antibody productivity of CHO-derived HBsAg protein at lower dose challenge was higher than the protein containing S region alone expressed in yeast system. These results indicate that CHO-derived HBsAg protein containing preS2 and S region can be effectively used for a better immune response as a HBV vaccine.

• Proceedings of the Korean Society for Bioinformatics Conference
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• 2002.06a
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• pp.5-23
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• 2002

Motivation: Protein-protein interaction plays a critical role in the biological processes. The identification of interacting proteins by bioinformatical methods can provide new lead In the functional studies of uncharacterized proteins without performing extensive experiments. Results: Protein-protein interactions are predicted by a computational algorithm based on the weighted scoring system for domain interactions between interacting protein pairs. Here we propose potential interaction domain (PID) pairs can be extracted from a data set of experimentally identified interacting protein pairs. where one protein contains a domain and its interacting protein contains the other. Every combinations of PID are summarized in a matrix table termed the PID matrix, and this matrix has proposed to be used for prediction of interactions. The database of interacting proteins (DIP) has used as a source of interacting protein pairs and InterPro, an integrated database of protein families, domains and functional sites, has used for defining domains in interacting pairs. A statistical scoring system. named "PID matrix score" has designed and applied as a measure of interaction probability between domains. Cross-validation has been performed with subsets of DIP data to evaluate the prediction accuracy of PID matrix. The prediction system gives about 50% of sensitivity and 98% of specificity, Based on the PID matrix, we develop a system providing several interaction information-finding services in the Internet. The system, named PreDIN (Prediction-oriented Database of Interaction Network) provides interacting domain finding services and interacting protein finding services. It is demonstrated that mapping of the genome-wide interaction network can be achieved by using the PreDIN system. This system can be also used as a new tool for functional prediction of unknown proteins.